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-Structure paper
Title | De novo sequence redesign of a functional Ras-binding domain globally inverted the surface charge distribution and led to extreme thermostability. |
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Journal, issue, pages | Biotechnol. Bioeng., Vol. 118, Page 2031-2042, Year 2021 |
Publish date | Dec 5, 2017 (structure data deposition date) |
Authors | Liu, R. / Wang, J. / Xiong, P. / Chen, Q. / Liu, H. |
External links | Biotechnol. Bioeng. / PubMed:33590881 |
Methods | NMR (solution) |
Structure data | PDB-5yxi: |
Source |
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Keywords | DE NOVO PROTEIN / Designed protein |